ID F6XCG4_MONDO Unreviewed; 504 AA. AC F6XCG4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 2. DT 13-SEP-2023, entry version 62. DE RecName: Full=Fumarate hydratase, mitochondrial {ECO:0000256|ARBA:ARBA00013409}; DE EC=4.2.1.2 {ECO:0000256|ARBA:ARBA00012921}; GN Name=FH {ECO:0000313|Ensembl:ENSMODP00000008696.3}; OS Monodelphis domestica (Gray short-tailed opossum). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Metatheria; Didelphimorphia; Didelphidae; Monodelphis. OX NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000008696.3, ECO:0000313|Proteomes:UP000002280}; RN [1] {ECO:0000313|Ensembl:ENSMODP00000008696.3, ECO:0000313|Proteomes:UP000002280} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17495919; DOI=10.1038/nature05805; RA Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S., RA Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M., RA Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V., RA Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E., RA Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A., RA Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S., RA Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E., RA Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K., RA VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C., RA Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P., RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A., RA Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M., RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K., RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J., RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A., RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R., RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L., RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C., RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L., RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F., RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T., RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J., RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S., RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I., RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., RA Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M., RA Samollow P.B., Lander E.S., Lindblad-Toh K.; RT "Genome of the marsupial Monodelphis domestica reveals innovation in non- RT coding sequences."; RL Nature 447:167-177(2007). RN [2] {ECO:0000313|Ensembl:ENSMODP00000008696.3} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2023) to UniProtKB. CC -!- FUNCTION: Catalyzes the hydration of fumarate to L-malate in the CC tricarboxylic acid (TCA) cycle to facilitate a transition step in the CC production of energy in the form of NADH. CC {ECO:0000256|ARBA:ARBA00003146}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2; CC Evidence={ECO:0000256|ARBA:ARBA00024594}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12461; CC Evidence={ECO:0000256|ARBA:ARBA00024594}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2; CC Evidence={ECO:0000256|ARBA:ARBA00024453}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12462; CC Evidence={ECO:0000256|ARBA:ARBA00024453}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate CC from fumarate: step 1/1. {ECO:0000256|ARBA:ARBA00004859}. CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase CC subfamily. {ECO:0000256|ARBA:ARBA00009084}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_001377948.1; XM_001377911.4. DR AlphaFoldDB; F6XCG4; -. DR STRING; 13616.ENSMODP00000008696; -. DR Ensembl; ENSMODT00000008868.4; ENSMODP00000008696.3; ENSMODG00000007014.4. DR GeneID; 100027739; -. DR KEGG; mdo:100027739; -. DR CTD; 2271; -. DR eggNOG; KOG1317; Eukaryota. DR GeneTree; ENSGT00950000183122; -. DR HOGENOM; CLU_021594_4_1_1; -. DR InParanoid; F6XCG4; -. DR OMA; HDSMGEV; -. DR OrthoDB; 1341425at2759; -. DR TreeFam; TF300441; -. DR UniPathway; UPA00223; UER01007. DR Proteomes; UP000002280; Chromosome 2. DR Bgee; ENSMODG00000007014; Expressed in skeletal muscle tissue and 18 other tissues. DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro. DR GO; GO:0004333; F:fumarate hydratase activity; IBA:GO_Central. DR GO; GO:0006106; P:fumarate metabolic process; IBA:GO_Central. DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl. DR GO; GO:0006108; P:malate metabolic process; IBA:GO_Central. DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl. DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central. DR CDD; cd01362; Fumarase_classII; 1. DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1. DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1. DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1. DR HAMAP; MF_00743; FumaraseC; 1. DR InterPro; IPR005677; Fum_hydII. DR InterPro; IPR024083; Fumarase/histidase_N. DR InterPro; IPR018951; Fumarase_C_C. DR InterPro; IPR020557; Fumarate_lyase_CS. DR InterPro; IPR000362; Fumarate_lyase_fam. DR InterPro; IPR022761; Fumarate_lyase_N. DR InterPro; IPR008948; L-Aspartase-like. DR NCBIfam; TIGR00979; fumC_II; 1. DR PANTHER; PTHR11444; ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE; 1. DR PANTHER; PTHR11444:SF1; FUMARATE HYDRATASE, MITOCHONDRIAL; 1. DR Pfam; PF10415; FumaraseC_C; 1. DR Pfam; PF00206; Lyase_1; 1. DR PRINTS; PR00145; ARGSUCLYASE. DR PRINTS; PR00149; FUMRATELYASE. DR SUPFAM; SSF48557; L-aspartase-like; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. PE 3: Inferred from homology; KW Reference proteome {ECO:0000313|Proteomes:UP000002280}. FT DOMAIN 52..383 FT /note="Fumarate lyase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00206" FT DOMAIN 449..501 FT /note="Fumarase C C-terminal" FT /evidence="ECO:0000259|Pfam:PF10415" SQ SEQUENCE 504 AA; 54026 MW; FD7D1CBA79D5CA6E CRC64; MYRSLRSVVL PLRLSQPSPL GPACATCTQL RPPIAARMAS QDSFRIEYDT FGELKVPSDK YYGAQTVRST LNFKIGGVTE RMPIPVIKAF GIFKRAAAEV NQDYGLDPKI ASAIVKAADE VAGGKLNDHF PLVVWQTGSG TQTNMNVNEV ISNRAIEILG GKLGSKDPVH PNDHVNKSQS SNDSFPTAMH IAAATEVHEV LLPGLQKLHD ALDAKSKEFA QIIKIGRTHT QDAVPLTLGQ EFSAYVQQIK YGMDRIKAAM PRVYELAAGG TAVGTGLNTR IGFAEKVAAK VASLTGLPFV TAPNKFEALA AHDALVELSG AMNTVACSLM KIANDIRFLG SGPRSGLGEL LLPENEPGSS IMPGKVNPTQ CEAVTMVAAQ VMGNHVAVTV GGSNGHFELN VFKPMIIKNV LNSARLLGDV SVSFTDNCVV GIQANTERIN KLMKESLMLV TALNPHIGYD KAAKIAKTAH KNGSTLKETA IELGYLTAEQ FDEWVKPKDM LGPK //